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Crystal Structure of Human ZAG, a Fat-Depleting Factor Related to MHC Molecules

Sánchez, Luis M. and Chirino, Arthur J. and Bjorkman, Pamela J. (1999) Crystal Structure of Human ZAG, a Fat-Depleting Factor Related to MHC Molecules. Science, 283 (5409). pp. 1914-1919. ISSN 0036-8075. doi:10.1126/science.283.5409.1914.

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Zn-α_2-glycoprotein (ZAG) is a soluble protein that is present in serum and other body fluids. ZAG stimulates lipid degradation in adipocytes and causes the extensive fat losses associated with some advanced cancers. The 2.8 angstrom crystal structure of ZAG resembles a class I major histocompatibility complex (MHC) heavy chain, but ZAG does not bind the class I light chain β_2-microglobulin. The ZAG structure includes a large groove analogous to class I MHC peptide binding grooves. Instead of a peptide, the ZAG groove contains a nonpeptidic compound that may be implicated in lipid catabolism under normal or pathological conditions.

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Bjorkman, Pamela J.0000-0002-2277-3990
Additional Information:© 1999 American Association for the Advancement of Science. Received 21 December 1998; accepted 18 February 1999. We thank G. Hathaway, P. G. Green, and K. Faull for mass spectrometric analyses. ZAG coordinates have been deposited in the PDB (code 1zag). L.M.S. was supported by a grant from the U.S. Department of Defense Breast Cancer Research Program.
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Department of Defense Breast Cancer Research ProgramUNSPECIFIED
Issue or Number:5409
Record Number:CaltechAUTHORS:20141121-150058081
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Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:52060
Deposited By: Tony Diaz
Deposited On:21 Nov 2014 23:16
Last Modified:10 Nov 2021 19:20

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